Binding of low mobility group protein from rat liver chromatin with histones studied by chemical cross-linking.
The protein of molecular weight about 160 kD (designated LMG160) was isolated from purified low mobility group chromatin proteins. Polyclonal antibody directed against the LMG160 protein in mouse was raised. The specificity of the antibody was determined with the use of ELISA. Using chemical cross-linking procedure followed by immunoprecipitation with the antiLMG160 antibody complex formation with chromatin proteins was demonstrated. Among the proteins that form complexes with LMG160, histones H3, H2A, and H4 were identified (Western blotting technique).
Wiland
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Institute of Human Genetics, Polish Academy of Sciences, Poznań, Poland.
Siemieniako
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Trzeciak
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D000818:Animals; D000906:Antibodies; D015153:Blotting, Western; D002843:Chromatin / Q000378:metabolism*; D002846:Chromatography, Affinity; D002868:Chromosomal Proteins, Non-Histone / Q000302:isolation & purification / Q000378:metabolism*; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D008970:Molecular Weight; D051381:Rats; D013388:Succinimides
D000906:Antibodies; D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D003432:Cross-Linking Reagents; D006657:Histones; D013388:Succinimides; C011240:dithiobis(succinimidylpropionate)